LIR motifs and the membrane-targeting domain are complementary in the function of RavZ

The bacterial effector protein RavZ is secreted by the intracellular pathogen Legionella pneumophila and inhibits host autophagy through an irreversible deconjugation of mammalian ATG8 (mATG8) proteins from autophagosome membranes. However, the roles of the LC3 interacting region (LIR) motifs in Rav...

Full description

Saved in:
Bibliographic Details
Published in:BMB reports 2019-12, Vol.52 (12), p.700-705
Main Authors: Park, Sang-Won, Jun, Yong-Woo, Jeon, Pureum, Lee, You-Kyung, Park, Ju-Hui, Lee, Seung-Hwan, Lee, Jin-A, Jang, Deok-Jin
Format: Article
Language:Korean
Subjects:
Autophagosome
LIR motif
MT domain
RavZ
Xenophagy
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The bacterial effector protein RavZ is secreted by the intracellular pathogen Legionella pneumophila and inhibits host autophagy through an irreversible deconjugation of mammalian ATG8 (mATG8) proteins from autophagosome membranes. However, the roles of the LC3 interacting region (LIR) motifs in RavZ function remain unclear. In this study, we show that a membrane-targeting (MT) domain or the LIR motifs of RavZ play major or minor roles in RavZ function. A RavZ mutant that does not bind to mATG8 delipidated all forms of mATG8-phosphatidylethanolamine (PE) as efficiently as did wild-type RavZ. However, a RavZ mutant with a deletion of the MT domain selectively delipidated mATG8-PE less efficiently than did wild-type RavZ. Taken together, our results suggest that the effects of LIR motifs and the MT domain on RavZ activity are complementary and work through independent pathways. [BMB Reports 2019; 52(12): 700-705]
ISSN:1976-6696
1976-670X